Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: Expression, localization and genetic interaction and physical associatiion with Gpa1 (the G-protein α subunit)

Molecular and Cellular Biology

Volumn 16, Issue 9, 1996, Pages 5194-5209

  Dohlman, Henrik G ^a,b   Song, Jianping ^a   Ma, Doreen ^b,c   Courchesne, William E ^b,d   Thorner, Jeremy ^b  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c ELI LILLY AND COMPANY   (United States)

^d UNIVERSITY OF NEVADA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; PHEROMONE; PROTEIN SUBUNIT; REGULATOR PROTEIN;

ARTICLE; HORMONE SENSITIVITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; REGULATOR GENE; REGULATORY MECHANISM; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

BOVINAE; SACCHAROMYCES CEREVISIAE;

EID: 0029767982     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.9.5194     Document Type: Article

References (127)

1. Arkinstall, S. J., S. G. Papasawas, and M. A. Payton. 1991. Y east α-mating factor receptor-linked G-protein signal transduction suppresses Ras-dependent activity. FEBS Lett. 284:123-128.
2. Arshavsky, V., and M. D. Bownds. 1992. Regulation of deactivation of photo-receptor G protein by its target enzyme and cGMP. Nature (London) 357:416-417.
3. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1987. Current protocols in molecular biology. Wiley-Interscience, New York.
4. Ballester, R., D. Marchuk, M. Boguski, A. Saulino, R. Letcher, M. Wigler, and F. Collins. 1990. The NFI locus encodes a protein functionally related to mammalian GAP and yeast IRA proteins. Cell 63:851-859.
5. Bardwell, L., J. G. Cook, C. J. Inouye, and J. Thorner. 1994. Signal propagation and regulation in the mating pheromone response pathway of the yeast Saccharomyces cerevisiae. Dev. Biol. 166:363-379.
6. Baum, P., J. Thorner, and L. Honig. 1978. Identification of tubulin from the yeast S. cerevisiae. Proc. Natl. Acad. Sci. USA 75:4962-4966.
7. Berstein, G., J. L. Blank, D. Y. Jhon, J. H. Exton, S. G. Rhee, and E. M. Ross. 1992. Phospholipase C-β1 is a GTPase-activating protein for Gq/11, its physiologic regulator. Cell 70:411-418.
8. Bhattacharya, S., L. Chen, J. R. Broach, and S. Powers. 1995. Ras membrane targeting is essential for glucose signaling but not for viability in yeast. Proc. Natl. Acad. Sci. USA 92:2984-2988.
9. Blinder, D., S. Bouvier, and D. D. Jenness. 1989. Constitutive mutants in the yeast pheromone response: ordered function of the gene products. Cell 56:479-486.
10. Blinder, D., and D. D. Jenness. 1989. Regulation of postreceptor signaling in the pheromone response pathway of Saccharomyces cerevisiae. Mol. Cell. Biol. 9:3720-3726.
11. Blumer, K. J., J. E. Reneke, W. E. Courchesne, and J. Thorner. 1988. Functional domains of a peptide hormone receptor: the α-factor receptor (STE2 gene product) of the yeast Saccharomyces cerevisiae. Cold Spring Harbor Symp. Quant. Biol. 53:591-603.
12. Blumer, K. J., J. E. Reneke, and J. Thorner. 1988. The STE2 gene product is the ligand-binding component of the α-factor receptor of Saccharomyces cerevisiae. J. Biol. Chem. 263:10836-10842.
13. Blumer, K. J., and J. Thorner. 1990. Beta and gamma subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the alpha subunit but are required for receptor coupling. Proc. Natl. Acad. Sci. USA 87:4363-4367.
14. Blumer, K. J., and J. Thorner. 1991. Receptor-G protein signaling in yeast. Annu. Rev. Physiol. 53:37-57.
15. Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5′-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 152:164-175.
16. Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature (London) 127:117-127.
17. Bowser, R., and P. Novick. 1991. Sec15 protein, an essential component of the exocytotic apparatus, is associated with the plasma membrane and with a soluble 19.5S particle. J. Cell Biol. 112:1117-1131.
18. Carlson, M., and D. Botstein. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28:145-154.
19. Cassel, D., F. Eckstein, M. Lowe, and Z. Selinger. 1979. Determination of the turn-off reaction for the hormone-activated adenylate cyclase. J. Biol. Chem. 254:9835-9838.
20. Chan, R. K., L. M. Melnick, L. C. Blair, and J. Thorner. 1983. Extracellular suppression allows mating by pheromone-deficient sterile mutants of Saccharomyces cerevisiae. J. Bacteriol. 155:903-906.
21. Chan, R. K., and C. A. Otte. 1982. Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a-factor and α-factor pheromones. Mol. Cell. Biol. 2:11-20.
22. Chan, R. K., and C. A. Otte. 1982. Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a-factor and α-factor pheromones. Mol. Cell. Biol. 2:21-29.
23. Chen, W. J., and M. G. Douglas. 1987. The role of protein structure in the mitochondrial import pathway. Analysis of the soluble F1-ATPase β-subunit precursor. I. Biol. Chem. 262:15598-15604.
24. Ciejek, E., and J. Thorner. 1979. Recovery of S. cerevisiae a cells from G1 arrest by a factor pheromone requires endopeptidase action. Cell 18:623-635.
25. Cole, G. M., and S. I. Reed. 1991. Pheromone-induced phosphorylation of a G protein β subunit in S. cerevisiae is associated with an adaptive response to mating pheromone. Cell 64:703-716.
26. Cole, G. M., D. E. Stone, and S. I. Reed. 1990. Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway. Mol. Cell. Biol. 10:510-517.
27. Courchesne, W. E., R. Kunisawa, and J. Thorner. 1986. Control of pheromone response in Saccharomyces cerevisiae: isolation of the SST2 gene. Yeast 2:S74.
28. Courchesne, W. E., R. Kunisawa, and J. Thorner. 1989. A putative protein kinase overcomes pheromone-induced arrest of cell cycling in S. cerevisiae. Cell 58:1107-1119.
29. De Vries, L., M. Mousli, A. Wurmser, and M. G. Farquhar. 1995. GAIP, a protein that specifically interacts with the trimeric protein Gαi3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. USA 92:11916-11920.
30. Dietzel, C., and J. Kurjan. 1987. Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone. Mol. Cell. Biol. 7:4169-4177.
31. Dietzel, C., and J. Kurjan. 1987. The yeast SCG1 gene: a Get-like protein implicated in the a- and α-factor response pathway. Cell 50:1001-1010.
32. Dohlman, H. G., D. Apaniesk, Y. Chen, J. Song, and D. Nusskern. 1995. Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:3635-3643.
33. Dohlman, H. G., P. Goldsmith, A. M. Spiegel, and J. Thorner. 1993. Pheromone action regulates G-protein a subunit myristoylation in the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90:9688-9692.
34. Dohlman, H. G., J. Thorner, M. G. Caron, and R. J. Lefkowitz. 1991. Model systems for the study of seven-transmembrane-segment receptors. Annu. Rev. Biochem. 60:653-688.
35. Druey, K. M., K. J. Blumer, V. H. Kang, and J. H. Kehrl. 1996. Inhibition of G protein-mediated MAP kinase activation by members of a novel mammalian gene family. Nature (London) 379:742-746.
36. Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
37. 2+-dependent serine protease. Proc. Natl. Acad. Sci. USA 86:1434-1438.
38. Fuller, R. S., A. J. Brake, and J. Thorner. 1989. Intracellular targeting and structural conservation of a prohormone-processing endoprotease. Science 246:482-486.
39. Gould, B., A. Salminen, N. C. Walworth, and P. J. Novick. 1988. A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast. Cell 53:753-768.
40. Graziano, M. P., and A. G. Gilman. 1989. Synthesis in Escherichia coli of GTPase-deficient mutants of Gs alpha. J. Biol. Chem. 264:15475-15482.
41. Guthrie, C., and G. R. Fink. 1991. Guide to yeast genetics and molecular biology. Academic Press, Inc., San Diego, Calif.
42. Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
43. Hartwell, L. H. 1980. Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J. Cell Biol. 85:811-822.
44. Hasson, M. S. 1992. Analysis of Saccharomyces cerevisiae pheromone response: biochemical and genetic characterization of the Ste5 protein. Ph.D. thesis. University of California, Berkeley.
45. Hasson, M. S., D. Blinder, J. Thorner, and D. D. Jenness. 1994. Mutational activation of the STES gene product bypasses the requirement for G protein β and γ subunits in the yeast pheromone response pathway. Mol. Cell. Biol. 14:1054-1065.
46. Hendricks, K. B., and J. Thorner. Unpublished results.
47. Herskowitz, I. 1995. MAP kinase pathways in yeast: for mating and more. Cell 80:187-197.
48. Hill, J. E., A. M. Myers, T. J. Koerner, and A. Tzagaloff. 1986 Yeast/E. coli shuttle vectors. Yeast 2:163-167.
49. Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
50. Jahng, K.-Y., J. Ferguson, and S. I. Reed. 1988. Mutations in a gene encoding the a subunit of a Saccharomyces cerevisiae G protein indicate a role in mating pheromone signaling. Mol. Cell. Biol. 8:2484-2493.
51. Jones, E. 1991. Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 194:428-453.
52. Julius, D., L. Blair, A. Brake, G. Sprague, and J. Thorner. 1983. Yeast α-factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32:839-852.
53. Kleuss, C., A. S. Raw, E. Lee, S. R. Sprang, and A. G. Gilman. 1994. Mechanism of GTP hydrolysis by G-protein alpha subunits. Proc. Natl. Acad. Sci. USA 91:9828-9831.
54. Koelle, M. R., and H. R. Horvitz. 1996. EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84:115-125.
55. Koerner, T. J., J. E. Hill, A. M. Myers, and A. Tzagoloff. 1991. High-expression vectors with multiple cloning sites for construction of UpE fusion genes: pATH vectors. Methods Enzymol. 194:477-490.
56. Konopka, J. B., D. D. Jenness, and L. H. Hartwell. 1988. The C-terminus of the S. cerevisiae α-pheromone receptor mediates an adaptive response to pheromone. Cell 54:609-620.
57. Kozasa, T., and A. G. Gilman. 1995. Purification of recombinant G proteins from Sf9 cells by hexahistidine tagging of associated subunits. Characterization of alpha-12 and inhibition of adenylyl cyclase by alpha-z. J. Biol. Chem. 270:1734-1741.
58. Kurjan, J. 1993. The pheromone response pathway in Saccharomyces cerevisiae. Annu. Rev. Genet. 27:147-179.
59. Kurjan, J., J. P. Hirsch, and C. Dietzel. 1991. Mutations in the guanine nucleotide-binding domains of a yeast Ga protein confer a constitutive or uninducible state to the pheromone response pathway. Genes Dev. 5:475-483.
60. Lacal, J. C., and F. McCormick. 1993. The ras superfamily of GTPases. CRC Press, Inc., Boca Raton, Fla.
61. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
62. Landis, C. A., S. B. Masters, A. Spada, A. M. Pace, H. R. Bourne, and L. Vallar. 1989. GTPase inhibiting mutations activate the a chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature (London) 340:692-696.
63. Lee, B. N., and T. H. Adams. 1994. Overexpression of flbA, an early regulator of Aspergillus asexual sporulation, leads to activation of brlA and premature initiation of development. Mol. Microbiol. 14:323-334.
64. Levin, D. E., and B. Errede. 1995. The proliferation of MAP kinase signaling pathways in yeast. Curr. Opin. Cell Biol. 7:197-202.
65. Lohse, M. J. 1993. Molecular mechanisms of membrane receptor desensitization. Biochim. Biophys. Acta 1179:171-188.
66. MacKay, V. L., J. Armstrong, C. Yip, S. Welch, K. Walker, S. Osborne, P. Sheppard, and J. Forstrom. 1991. Characterization of the Bar proteinase, an extracellular enzyme from the yeast Saccharomyces cerevisiae. Adv. Exp. Med. Biol. 306:161-172.
67. MacKay, V. L., S. K. Welch, M. Y. Insley, T. R. Manney, J. Holly, G. C. Saari, and M. L. Parker. 1988. The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin. Proc. Natl. Acad. Sci. USA 85:55-59.
68. Madura, K., and A. Varshavsky. 1994. Degradation of G alpha by the N-end rule pathway. Science 265:1454-1458.
69. Markby, D. W., R. Onrust, and H. R. Bourne. 1993. Separate GTP binding and GTPase activating domains of a G alpha subunit. Science 262:1895-1901.
70. Marsh, L., and I. Herskowitz. 1988. From membrane to nucleus: the pathway of signal transduction in yeast and its genetic control. Cold Spring Harbor Symp. Quant. Biol. 53:557-566.
71. Marshall, M. S., W. S. Hill, S. N. Assunta, U. S. Vogel, M. D. Schaber, E. M. Scolnick, R. A. F. Dixon, I. S. Sigal, and J. B. Gibbs. 1989. A C-terminal domain of GAP is sufficient to stimulate ras p21 GTPase activity. EMBO J. 8:1105-1110.
72. Martin, G. A., D. Viskochil, G. Bollag, P. C. McCabe, W. J. Crosier, H. Haubruck, L. Conroy, R. Clark, P. O'Connell, R. M. Cawthon, et al. 1990. The GAP-related domain of the neurofibromatosis type 1 gene product interacts with ras p21. Cell 63:843-849.
73. Masters, S. B., R. T. Miller, M. H. Chi, F. H. Chang, B. Beiderman, N. G. Lopez, and H. R. Bourne. 1989. Mutations in the GTP-binding site of Gs alpha alter stimulation of adenylyl cyclase. J. Biol. Chem. 264:15467-15474.
74. Milligan, G. 1993. Agonist regulation of cellular G protein levels and distribution: mechanisms and functional implications. Trends. Pharmacol. Sci. 14:413-418.
75. VAL-50 mutation in the mating-factor signaling pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:2289-2297.
76. Miyajima, I., M. Nakafuku, N. Nakayama, C. Brenner, A. Miyajima, K. Kaibuchi, K. I. Arai, Y. Kaziro, and K. Matsumoto. 1987. GPA1, a haploid-specific essential gene, encodes a yeast homolog of mammalian G protein which may be involved in the mating factor-mediated signal transduction pathway. Cell 50:1011-1019.
77. Miyajima, I., N. Nakayama, M. Nakafuku, Y. Kaziro, K. Arai, and K. Matsumoto. 1988. Suppressors of a gpa1 mutation cause sterility in Saccharomyces cerevisiae. Genetics 119:797-804.
78. Moore, S. A. 1984. Yeast cells recover from mating pheromone α-factor-induced division arrest by desensitization in the absence of α-factor destruction. J. Biol. Chem. 259:1004-1010.
79. Nomoto, S., N. Nakayama, K. Arai, and K. Matsumoto. 1990. Regulation of the yeast pheromone response pathway by G protein subunits. EMBO J. 9:691-696.
80. Oehlen, B., and F. R. Cross. 1994. Signal transduction in the budding yeast, Saccharomyces cerevisiae. Curr. Opin. Cell Biol. 6:836-841.
81. Papasavvas, S., S. Arkinstall, J. Reid, and M. Payton. 1992. Yeast alpha-mating factor receptor and G-protein-linked adenylyl cyclase inhibition requires RAS2 and GPA2 activities. Biochem. Biophys. Res. Commun. 184: 1378-1385.
82. Pennington, S. R. 1994. GTP-binding proteins: heterotrimeric G proteins, p. 169-356. In P. Sheterline (ed.), Prolein profiles. Vol. 1. Academic Press, Ltd., London.
83. Peterson, J., Y. Zheng, L. Bender, A. Myers, R. Cerione, and A. Bender. 1994. Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast. J. Cell Biol. 127:1395-1406.
84. Pimplikar, S. W., and K. Simons. 1993. Regulation of apical transport in epithelial cells by a Gs class of heterotrimeric G protein. Nature (London) 362:456-458.
85. Pringle, J. R., A. E. M. Adams, D. G. Drubin, and B. K. Haarer. 1991. Immunofluorescence methods for yeast. Methods Enzymol. 194:565-602.
86. Redding, K., C. Holcomb, and R. S. Fuller. 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell Biol. 113:527-538.
87. Reneke, J. E., K. J. Blumer, W. E. Courchesne, and J. Thorner. 1988. The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain. Cell 55:221-234.
88. Rogers, S., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
89. Roush, W. 1996. Regulating G protein signaling. Science 271:1056-1058.
90. 1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 14:7953-7966.
91. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
92. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
93. Schandel, K. A., and D. D. Jenness. 1994. Direct evidence for ligand-induced internalization of the yeast ex-factor pheromone receptor. Mol. Cell. Biol. 14:7245-7255.
94. Scherer, S., and R. W. Davis. 1979. Replacement of chromosome segments with altered DNA sequences constructed in vitro. Proc. Natl. Acad. Sci. USA 76:4951-4955.
95. Schultz, J., B. Ferguson, and G. F. Sprague, Jr. 1995. Signal transduction and growth control in yeast. Curr. Opin. Genet. Dev. 5:31-37.
96. Sherman, F., G. R. Fink, and J. A. Hicks. 1986. Laboratory course manual for methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
97. Siderovski, D. P., A. Hessel, S. Chung, T. M. Mak, and M. Tyers. 1996. A new family of G protein-coupled receptor regulators? Curr. Biol. 6:211-212.
98. Simon, M. N., C. De Virgilio, B. Souza, J. R. Pringle, A. Abo, and S. I. Reed. 1995. Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway. Nature (London) 376:702-705.
99. Song, J., K. Gunn, and H. G. Dohlman. 1995. Regulation of cell membrane polarity by a heterotrimeric G protein, p. 272. In Abstracts of the Yeast Cell Biology Meeting. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
100. Song, J., J. Hirschman, K. Gunn, and H. G. Dohlman. Regulation of membrane and subunit interactions by N-myristoylation of a G protein a subunit in yeast. J. Biol. Chem., in press.
101. Sprague, G. F., Jr. 1991. Assay of yeast mating reaction. Methods Enzymol. 194:21-37.
102. Sprague, G. F., Jr., and J. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae, p. 657-744. In J. R. Broach, J. R. Pringle, and E. W. Jones (ed.), The molecular and cellular biology of the yeast Saccharomyces. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
103. Stirling, C. J., J. Rothblatt, M. Hosobuchi, R. Deshaies, and R. Schekman. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell. 3:129-142.
104. Stone, D. E., G. M. Cole, M. de Barros Lopes, M. Goebl, and S. I. Reed. 1991. N-Myristoylation is required for function of the pheromone-responsive Ga protein of yeast: conditional activation of the pheromone response by a temperature-sensitive N-myristoyl transferase. Genes Dev. 5:1969-1981.
105. Stone, D. E., and S. I. Reed. 1990. G protein mutations that alter the pheromone response in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:4439-4446.
106. Strahl, K., D. Stinchcomb, S. Scherer, and R. W. Davis. 1979. High frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc. Natl. Acad. Sci. USA 76:1035-1039.
107. Tan, P. K., N. G. Davis, G. F. Sprague, Jr., and G. S. Payne. 1993. Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast. J. Cell Biol. 123:1707-1716.
108. Tanaka, K., M. Nakafuku, T. Satoh, M. S. Marshall, J. S. Gibb, K. Matsumoto, Y. Kaziro, and A. Toh-e. 1990. S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase-activating protein. Cell 60:803-807.
109. Tongaonkar, P., and K. Madura. Personal communication.
110. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
111. Trahey, M., G. Wong, R. Halenbeck, B. Rubinfeld, G. A. Martin, M. Ladner, C. M. Long, W. J. Crosier, K. Watt, and K. Koths. 1988. Molecular cloning of two types of GAP complementary DNA from human placenta. Science 242:1697-1700.
112. Van Dop, C., M. Tsubokawa, H. R. Bourne, and J. Ramachandran. 1984. Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem. 259:696-698.
113. Weiner, J. L., C. Guttieriez-Steil, and K. J. Blumer. 1993. Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaptation pathway. J. Biol. Chem. 268:8070-8077.
114. Whiteway, M., K. L. Clark, E. Leberer, D. Dignard, and D. Y. Thomas. 1994. Genetic identification of residues involved in association of α and β G-protein subunits. Mol. Cell. Biol. 14:3223-3229.
115. Whiteway, M., L. Hougan, D. Dignard, D. Y. Thomas, L. Bell, G. C. Saari, F. J. Grant, P. O'Hara, and V. L. MacKay. 1989. The STE4 and STE18 genes of yeast encode potential β and γ subunits of the mating factor receptor-coupled G protein. Cell 56:467-477.
116. Whiteway, M., L. Hougan, and D. Y. Thomas. 1988. Expression of MFα1 in MATa cells supersensitive to α-factor leads to self arrest. Mol. Gen. Genet. 214:85-88.
117. Whiteway, M., L. Hougan, and D. Y. Thomas. 1990. Overexpression of the STE4 gene leads to mating response in haploid Saccharomyces cerevisiae. Mol. Cell. Biol. 10:217-222.
118. Whiteway, M., and D. Y. Thomas. 1994. Site-directed mutations altering the CAAX box of Ste18, the yeast pheromone-response pathway Gγ subunit. Genetics 137:967-976.
119. Wilson, B. S., M. Komuro, and M. G. Farquhar. 1994. Cellular variations in heterotrimeric G protein localization and expression in rat pituitary. Endocrinology 134:233-244.
120. Wu, H.-K., H. H. Q. Heng, X.-M. Shi, D. R Forsdyke, L.-C. Tsui, T. W. Mak, M. D. Minden, and D. P. Siderovski. 1995. Differential expression of a basic helix-loop-helix phosphoprotein gene, GOS8, in acute leukemia and localization to human chromosome 1q31. Leukemia 9:1291-1298.
121. Xu, G. F., B. Lin, K. Tanaka, D. Dunn, D. Wood, R. Gesteland, R. White, R. Weiss, and F. Tamanol. 1990. The catalytic domain of the neurofibromatosis type 1 gene product stimulates ras GTPase and complements ira mutants of S. cerevisiae. Cell 63:843-849.
122. Xu, G. F., P. O'Connell, D. Viskochil, R. Cawthon, M. Robertson, M. Culver, D. Dunn, J. Stevens, R. Gesteland, and R. White. 1990. The neurofibromatosis type 1 gene encodes a protein related to GAP. Cell 62:599-608.
123. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
124. Zhao, Z.-S., T. Leung, E. Manser, and L. Lim. 1995. Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24. Mol. Cell. Biol. 15:5246-5257.
125. Zheng, Y., R. Cerione, and A. Bender. 1994. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J. Biol. Chem. 269: 2369-2372.
126. Zheng, Y., M. J. Hart, K. Shinjo, T. Evans, A. Bender, and R. A. Cerione. 1993. Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain. J. Biol. Chem. 268:24629-24634.
127. Ziman, M., D. Preuss, J. Mulholland, J. M. O'Brien, D. M. Botstein, and D. I. Johnson. 1993. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell 4:1307-1316.